Acrosin shows zona and fucose binding, novel properties for a serine proteinase
- 21 December 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 226 (1) , 38-42
- https://doi.org/10.1016/0014-5793(87)80546-x
Abstract
The major fucose-binding protein of 53 kDa from boar spermatozoa was isolated to apparent homogeneity using a two-step procedure including high-performance gel filtration and reversed-phase chromatography. The N-terminal sequence of the protein revealed that it is identical with the sperm proteinase acrosin. By means of a solid-phase zona-binding assay based on the avidin-biotin system it was demonstrated that acrosin also interacts strongly with porcine zona pellucida. Thus, the acrosin molecule combines specific proteolytic activity with zona- and carbohydrate-affinity properties, i.e. previously unrecognized properties of a serine proteinase. It seems likely that this special affinity of acrosin directs the proteolytic activity to its structural target in the vivo situation.Keywords
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